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4hly

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==The complex crystal structure of the DNA binding domain of vIRF-1 from the oncogenic KSHV with DNA==
==The complex crystal structure of the DNA binding domain of vIRF-1 from the oncogenic KSHV with DNA==
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<StructureSection load='4hly' size='340' side='right' caption='[[4hly]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
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<StructureSection load='4hly' size='340' side='right'caption='[[4hly]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4hly]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hhv-8 Hhv-8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HLY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HLY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4hly]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_8 Human gammaherpesvirus 8] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HLY FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF K9, vIRF, vIRF-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37296 HHV-8])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hly OCA], [http://pdbe.org/4hly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hly RCSB], [http://www.ebi.ac.uk/pdbsum/4hly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hly ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hly OCA], [https://pdbe.org/4hly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hly RCSB], [https://www.ebi.ac.uk/pdbsum/4hly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hly ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/VIRF1_HHV8P VIRF1_HHV8P] Plays a role in the inhibition of host innate response by repressing the expression of interferon-inducible genes and blocking host IRF1- and IRF3-mediated transcription. Blocks the interaction between host IRF3 and CREBBP. Regulates the host cellular metabolism by increasing glucose uptake, ATP production and lactate secretion through down-regulation of heterogeneous nuclear ribonuclear protein Q1/SYNCRIP. Mechanistically, induces ubiquitination and degradation of SYNCRIP through the ubiquitin-proteasome pathway by recruiting KLHL3/CUL3 ubiquitin ligase complex (PubMed:35538151). Disrupts host TP53 signaling pathway during viral infection by interacting with host USP7 and thereby decreasing the availability of USP7 for deubiquitinating and stabilizing TP53 (PubMed:26786098).<ref>PMID:11314014</ref> <ref>PMID:26786098</ref> <ref>PMID:35538151</ref> <ref>PMID:9365244</ref> <ref>PMID:9420276</ref>
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Kaposi's sarcoma-associated herpesvirus encodes four viral homologues to cellular interferon regulatory factors (IRFs), where the most studied is vIRF-1. Even though vIRF-1 shows sequence homology to the N-terminal DNA-binding domain (DBD) of human IRFs, a specific role for this domain in vIRF-1's function has remained uncertain. To provide insights into the function of the vIRF-1 DBD, we have determined the crystal structure of it in complex with DNA and in its apo-form. Using a thermal stability shift assay (TSSA), we show that the vIRF-1 DBD binds DNA, whereas full-length vIRF-1 does not, suggesting a cis-acting regulatory mechanism in similarity to human IRFs. The complex structure of vIRF-1 DBD reveals interactions with the DNA backbone and the positioning of two arginines for specific recognition in the major grove. A superimposition with human IRF-3 reveals a similar positioning of the two specificity-determining arginines, and additional TSSAs indicate binding of vIRF-1 to an IRF-3 operator consensus sequence. The results from this study, therefore, provide support that vIRF-1 has evolved to bind DNA and plays a role in DNA binding in the context of transcriptional regulation and might act on some of the many operator sequences controlled by human IRF-3.
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The crystal structure of the DNA-binding domain of vIRF-1 from the oncogenic KSHV reveals a conserved fold for DNA binding and reinforces its role as a transcription factor.,Hew K, Dahlroth SL, Venkatachalam R, Nasertorabi F, Lim BT, Cornvik T, Nordlund P Nucleic Acids Res. 2013 Feb 21. PMID:23435230<ref>PMID:23435230</ref>
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==See Also==
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*[[Interferon regulatory factor|Interferon regulatory factor]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4hly" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hhv-8]]
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[[Category: Human gammaherpesvirus 8]]
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[[Category: Hew, K]]
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[[Category: Large Structures]]
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[[Category: Venkatachalam, R]]
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[[Category: Synthetic construct]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Hew K]]
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[[Category: Helix-turn-helix]]
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[[Category: Venkatachalam R]]

Current revision

The complex crystal structure of the DNA binding domain of vIRF-1 from the oncogenic KSHV with DNA

PDB ID 4hly

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